Ingredient Functionality During Foam-Type Cake Making: A Review.

Foam-type cakes are complex food systems. Their main ingredients are wheat flour, hen eggs, sugar, leavening agent, and, in some cases, oil and/or surfactants. In contrast to the vast amount of research outcomes on the contribution of ingredients to the quality of batter-type cake systems, information on the functionality and importance of the ingredients and their constituents in foam-type cake systems is lacking. This review defines foam-type cakes, describes how they are made, summarizes the current knowledge of factors determining their quality, and identifies the current knowledge gaps.

Sucrose substitution in cake systems is not a piece of cake.

Successful sucrose replacement in cake systems requires thorough understanding of its functionality. Time-domain 1H NMR showed that water in the viscous aqueous phase isolated from cake batter by ultracentrifugation [i.e. the batter liquor (BL)] exhibits low mobility by its low T2 relaxation time (T2,D RT). This is due to its interactions with sucrose or sucrose replacers. The T2,D RT itself is positively related with the effective volumetric hydrogen bond density of sucrose or sucrose replacers. Sucrose additionally co-determines the quantity and viscosity of cake BL and thereby how much air the batter contains at the end of mixing. Like sucrose, maltitol and oligofructose provide adequate volumes of BL with low water mobility and thus sufficient air in the batter, while the rather insoluble mannitol and inulin do not. Differential scanning calorimetry and rapid viscosity analysis revealed, however, that, in contrast to sucrose and maltitol, oligofructose fails to provide appropriate timings of starch gelatinisation and protein denaturation, resulting in poor cake texture. The shortcomings of mannitol and oligofructose in terms of respectively ensuring appropriate gas content in batter and biopolymer transitions during baking can be overcome by using mixtures thereof. This work shows that successful sucrose substitutes or substitute mixtures must provide sufficient BL with low water mobility and ensure appropriate timings of starch and protein biopolymer transitions during baking.

Hydrothermal Treatments Cause Wheat Gluten-Derived Peptides to Form Amyloid-like Fibrils.

Formation of amyloid fibrils (i.e., protein structures containing a compact core of ordered ß-sheet structures) from food proteins can improve their techno-functional properties. Wheat gluten is the most consumed cereal protein by humans and extensively present in food and feed systems. Hydrolysis of wheat gluten increases the solubility of its proteins and brings new opportunities for value creation. In this study, the formation of amyloid-like fibrils (ALFs) from wheat gluten peptides (WGPs) under food relevant processing conditions was investigated. Different hydrothermal treatments were tested to maximize the formation of straight ALFs from WGPs. Thioflavin T (ThT) fluorescence measurements and transmission electron microscopy (TEM) were performed to study the extent of fibrillation and the morphology of the fibrils, respectively. First, the formation of fibrils by heating solutions of tryptic WGPs [degrees of hydrolysis 2.0% (DH 2) or 6.0% (DH 6)] was optimized using a response surface design. WGP solutions were incubated at different pH values, times, and temperatures. DH 6 WGPs had a higher propensity for fibrillation than did DH 2 WGPs. Heating DH 6 WGPs at 2.0% (w/v) for 38 h at 85 °C and pH 7.0 resulted in optimal fibrillation. Second, trypsin, chymotrypsin, thermolysin, papain, and proteinase K were used to produce different DH 6 WGPs. After enzyme inactivation and subsequent heating at optimal fibrillation conditions, chymotrypsin and proteinase K DH 6 WGPs produced small worm-like fibrils, whereas fibrils prepared from trypsin DH 6 WGPs were long and straight. The surface hydrophobicity of the peptides was key for fibrillation. Third, peptides from the wheat gluten components gliadin and glutenin fractions formed smaller and worm-like fibrils than did WGPs. Thus, the peptides of both gluten protein fractions jointly contribute to gluten fibrillation.